Bioorganicheskaia khimiia 1995-01-01

[Solid-phase enzymatic reactions. V. Comparison of catalytic properties of subtilisin and alpha-chymotrypsin in the absence of a solvent].

E Iu Maksareva, Iu I Khurgin

Index: Bioorg. Khim. 21(1) , 24-7, (1995)

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Abstract

Subtilisin Carlsberg (E.C. 3.4.21.14) catalyzes the hydrolysis of N-succinyl-L-phenylalanine p-nitroanilide in solid-state solvent-free hydrated protein-substrate mixtures. This process needs a certain critical degree of hydration of the protein molecule which is attained at the relative water vapour pressure (p/ps) above 0.49. The identical hydration dependency was found for the solid-state inactivation of subtilisin by phenylmethylsulphonylfluoride. Despite the fact that subtilisin and alpha-chymotrypsin belong to two different families of serine proteinases, the characteristics of their solid-state catalytic reactions are almost identical.